Information on EC 1.14.19.3 - acyl-CoA 6-desaturase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
1.14.19.3
-
RECOMMENDED NAME
GeneOntology No.
acyl-CoA 6-desaturase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
alpha-linolenoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = stearidonoyl-CoA + 2 ferricytochrome b5 + 2 H2O
show the reaction diagram
linoleoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = gamma-linolenoyl-CoA + 2 ferricytochrome b5 + 2 H2O
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
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redox reaction
-
-
-
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reduction
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-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
(4Z,7Z,10Z,13Z,16Z)-docosapentaenoate biosynthesis (6-desaturase)
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-
docosahexaenoate biosynthesis III (6-desaturase, mammals)
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gamma-linolenate biosynthesis II (animals)
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icosapentaenoate biosynthesis II (6-desaturase, mammals)
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Linoleic acid metabolism
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Biosynthesis of unsaturated fatty acids
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Metabolic pathways
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-
SYSTEMATIC NAME
IUBMB Comments
linoleoyl-CoA,hydrogen-donor:oxygen oxidoreductase
An iron protein. The enzyme introduces a cis double bond at carbon 6 of acyl-CoAs. It is a front-end desaturase, introducing the new double bond between a pre-existing double bond and the carboxyl-end of the fatty acid. The human enzyme has a broad substrate range. It also acts on palmitoyl-CoA, generating sapienoyl-CoA [4], and on (9Z,12Z,15Z,18Z,21Z)-tetracosa-9,12,15,18,21-pentaenoyl-CoA, converting it to (6Z,9Z,12Z,15Z,18Z,21Z)-tetracosa-6,9,12,15,18,21-hexaenoyl-CoA as part of a pathway that produces docosahexaenoate [3]. The enzyme contains a cytochrome b5 domain that is assumed to act in vivo as the electron donor to the active site of the desaturase.
CAS REGISTRY NUMBER
COMMENTARY hide
9014-34-0
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
Heynh
-
-
Manually annotated by BRENDA team
gene fat-3
-
-
Manually annotated by BRENDA team
-
Q3LU33
UniProt
Manually annotated by BRENDA team
-
Q3LU33
UniProt
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
soybean, cv Tracy
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-
Manually annotated by BRENDA team
linseed, cultivar Punjab
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-
Manually annotated by BRENDA team
gene PiDesD6
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
-
K9L0F6
UniProt
Manually annotated by BRENDA team
-
K9L0F6
UniProt
Manually annotated by BRENDA team
gene ObD6Des
UniProt
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
; DELTA6-desaturase
SwissProt
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
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Q8AY64
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
metabolism
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(9Z,12Z,15Z,18Z,21Z)-tetracosa-9,12,15,18,21-pentaenoic acid + AH2 + O2
(6Z,9Z,12Z,15Z,18Z,21Z)-tetracosa-6,9,12,15,18,21-hexaenoic acid + A + H2O
show the reaction diagram
-
-
-
-
?
24-carbon fatty acid + AH2 + O2
? + A + H2O
show the reaction diagram
alpha-linolenic acid + AH2 + O2
(6Z,9Z,12Z,15Z)-octadeca-6,9,12,15-tetraenoic acid + A + H2O
show the reaction diagram
preferred substrate
-
-
?
alpha-linolenic acid + AH2 + O2
?
show the reaction diagram
alpha-linolenic acid + AH2 + O2
octadec-6,9,12,15-tetraenoic acid + A + H2O
show the reaction diagram
alpha-linolenic acid + AH2 + O2
octadeca-6,9,12,15-tetraenoic acid + A + H2O
show the reaction diagram
-
-
-
?
alpha-linolenic acid + AH2 + O2
octadecatetraenoic acid + A + H2O
show the reaction diagram
-
-
-
-
?
alpha-linolenic acid + AH2 + O2
stearidonic acid + A + H2O
show the reaction diagram
alpha-linolenoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
stearidonoyl-CoA + 2 ferricytochrome b5 + 2 H2O
show the reaction diagram
alpha-linolenoyl-CoA + ferrocytochrome b5 + O2 + H+
stearidonoyl-CoA + ferricytochrome b5 + H2O
show the reaction diagram
alpha-linoleoyl-CoA + AH2 + O2
stearidonoyl-CoA + A + 2 H2O
show the reaction diagram
gamma-linoleic acid + AH2 + O2
gamma-linolenic acid + A + H2O
show the reaction diagram
-
39% conversion efficiency
-
-
?
gamma-linolenic acid + AH2 + O2
cis-6,9,12,15-octadecatetraenoic acid + A + H2O
show the reaction diagram
-
-
-
-
?
gamma-linolenic acid methyl ester + O2
?
show the reaction diagram
heptadec-9-enoic acid + AH2 + O2
heptadec-6,9-dienoic acid + A + H2O
show the reaction diagram
-
conversion rate is 17%
-
-
?
linoleic acid + AH2 + O2
?
show the reaction diagram
linoleic acid + AH2 + O2
gamma-linoleic acid + A + H2O
show the reaction diagram
-
-
-
-
?
linoleic acid + AH2 + O2
gamma-linolenic acid + A + H2O
show the reaction diagram
linolenic acid + AH2 + O2
arachidonic acid + A + H2O
show the reaction diagram
linoleoyl phosphatidylcholine + AH2 + O2
gamma-linolenoylphosphatidylcholine + A + H2O
show the reaction diagram
-
-
-
-
?
linoleoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
gamma-linolenoyl-CoA + 2 ferricytochrome b5 + 2 H2O
show the reaction diagram
linoleoyl-CoA + AH2 + O2
gamma-linolenoyl-CoA + A + 2 H2O
show the reaction diagram
linoleoyl-CoA + ferrocytochrome b5 + O2 + H+
gamma-linolenoyl-CoA + ferricytochrome b5 + H2O
show the reaction diagram
monogalactosydiacylglycerol + AH2 + O2
? + A + H2O
show the reaction diagram
octadec-9,12-dienoic acid + AH2 + O2
octadec-6,9,12-trienoic acid + A + H2O
show the reaction diagram
-
conversion rate is 11.5%
-
-
?
octadec-9-enoic acid + AH2 + O2
octadec-6,9-dienoic acid + A + H2O
show the reaction diagram
-
conversion rate is 19.1%
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-
?
octadeca-9,12-dienoic acid + AH2 + O2
gamma-linolenic acid + A + H2O
show the reaction diagram
octadecanoate + AH2 + O2
? + A + H2O
show the reaction diagram
oleic acid + AH2 + O2
?
show the reaction diagram
-
-
-
-
?
palmitate + AH2 + O2
sapienate + A + H2O
show the reaction diagram
palmitic acid + AH2 + O2
hexadec-6-enoic acid + A + H2O
show the reaction diagram
palmitoyl-[acyl-carrier protein] + reduced acceptor + O2
6-hexadecenoyl-[acyl-carrier protein] + acceptor + H2O
show the reaction diagram
-
-
-
?
stearoyl-[acyl-carrier protein] + reduced acceptor + O2
6-octadecenoyl-[acyl-carrier protein] + 9-octadecenoyl-[acyl-carrier protein]acceptor + H2O
show the reaction diagram
-
-
ratio of activity: 2/1
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
alpha-linolenic acid + AH2 + O2
octadec-6,9,12,15-tetraenoic acid + A + H2O
show the reaction diagram
alpha-linolenoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
stearidonoyl-CoA + 2 ferricytochrome b5 + 2 H2O
show the reaction diagram
alpha-linolenoyl-CoA + ferrocytochrome b5 + O2 + H+
stearidonoyl-CoA + ferricytochrome b5 + H2O
show the reaction diagram
alpha-linoleoyl-CoA + AH2 + O2
stearidonoyl-CoA + A + 2 H2O
show the reaction diagram
E1U2Q3
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-
-
?
linoleic acid + AH2 + O2
gamma-linolenic acid + A + H2O
show the reaction diagram
linoleoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
gamma-linolenoyl-CoA + 2 ferricytochrome b5 + 2 H2O
show the reaction diagram
linoleoyl-CoA + AH2 + O2
gamma-linolenoyl-CoA + A + 2 H2O
show the reaction diagram
E1U2Q3
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-
-
?
linoleoyl-CoA + ferrocytochrome b5 + O2 + H+
gamma-linolenoyl-CoA + ferricytochrome b5 + H2O
show the reaction diagram
palmitate + AH2 + O2
sapienate + A + H2O
show the reaction diagram
O95864
the enzyme is a component of the lipid metabolic pathway that converts the essential fatty acids linoleate and alpha-linolenate into long-chain polyunsaturated fatty acids. The DELTA-6 desaturase/FADS2 expressed in human sebocytes catalyzes the conversion of palmitate into sapienate
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-
?
palmitic acid + AH2 + O2
hexadec-6-enoic acid + A + H2O
show the reaction diagram
-
key enzyme required for numerous vital functions involving distinct polyunsaturated fatty acids and polyunsaturated fatty acid-derived bioactive lipids. It seems that the biological importance of DELTA6-desaturase activity should also be considered for its newly identified role in the control of the biosynthesis of a monoenoic fatty acid (C16:1 n-10), particularly in tissues with low DELTA9-desaturase activity
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-
?
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cytochrome b5
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Ferredoxin
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heme
Q3LU33;
contains a cytochrome b5 heme-binding domain
linoleoyl-CoA
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absolutely essential for DELTA6-desaturation
NADH
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absolutely essential for DELTA6-desaturation
NADPH
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absolutely essential for DELTA6-desaturation
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe2+
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DELTA6-desaturase contains 15.1 nmol iron/mg protein
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-chloro-5-dimethylamino-2-phenyl-3(2H)-pyridazinone
bathophenanthroline sulfonate
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mild inhibition
beta-mercaptoethanol
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mild inhibition
cholesterol
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conjugated linoleic acid
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all CLA isomers inhibits significantly the activity of DELTA6-desaturase, the c9,t11 isomer is the most potent inhibitor
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CP-24879
F2WWK6;
the combined DELTA5 desaturase/DELTA6 desaturase inhibitor significantly reduces intracellular lipid accumulation and inflammatory injury in hepatocytes
dithiothreitol
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mild inhibition
Iron chelators
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N-ethylmaleimide
p-chloromercuribenzene sulfonate
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saturated fatty acids
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trans-fats
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additional information
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aging, diabetes, viral infection, high alcohol intake, high level cholesterol, high blood pressure, radiation, stress-related hormones, deficiencies of zinc, magnesium, biotin, the vitamins C, B6, and B3, and excessive level of trans fatty acid reduce the enzyme activity in vivo
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
bovine serum albumin
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1-10 mg/ml, stimulates enzyme activity of unwashed microsomes by 50%
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catalase
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NADH-cytochrome b5 reductase
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EC 1.6.2.2, absolutely essential for DELTA6-desaturation
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NADPH-cytochrome b5 reductase
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EC 1.6.2.2, absolutely essential for DELTA6-desaturation
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O2
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absolutely essential for DELTA6-desaturation
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.045
linoleoyl-CoA
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-
additional information
additional information
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.1
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substrate palmitoyl-[acyl-carrier protein]
additional information
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0.3 mM exogenously added NADPH to Escherichia coli cells co-expressing DELTA6 desaturase and cytochrome b5 leads to an increase of the level of gamma-linoleic acid product by 50%, but no effect in Escherichia coli co-expressing DELTA6 desaturase and ferredoxin under the same conditions; co-addition of NADPH and FAD to Escherichia coli cells co-expressing DELTA6 desaturase and ferredoxin leads to an increase of the level of gamma-linoleic acid product; no activity when expressed in Escherichia coli alone, co-expression of cytochrome b5 is needed
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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skin fibroblast
Manually annotated by BRENDA team
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much lower activity than in Sertoli cells
Manually annotated by BRENDA team
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-
Manually annotated by BRENDA team
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treatment with myristic acid specifically increases DELTA6-desaturase activity
Manually annotated by BRENDA team
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mRNA level is upregulated by dexamethasone, follicle-stimulating hormone or cAMP
Manually annotated by BRENDA team
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-
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45000
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recombinant DELTA6-desaturase expressed in COS-7 cells, analysed by Western blot
47000
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Western Blot, detection of histidine-tagged DELTA6 desaturase expressed in Escherichia coli using a monoclonal antibody against the histidine-tag
51800
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x * 51800, calculated from amino acid sequence
52000
Q3LU33;
calculated from amino acid sequence
65000 - 68000
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gel filtration
66000
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SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospholipoprotein
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70°C, stored under nitrogen the enzyme is unstable, loses 80% of its activity after repeated freezing and thawing
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15°C, full-length enzyme in 100 mM sodium phosphate, pH 7.0, 4 h, 16% loss of activity
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
D6D, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis; D6D-V, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis
B1PJR8;, B2ZE91;
DELTA6-desaturase gene identified in human chromosome 11
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DELTA6-desaturase II cDNA expressed in Aspergillus oryzae
DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, functional expression in Saccharomyces cerevisiae strain INVSc1
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expressed in Camelina sativa
expressed in Escherichia coli DH5alpha, co-expressed with cytochrome b5 and ferredoxin, no enzyme activity when expressed in Escherichia coli alone
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expressed in HEK-293 cells
expressed in Pichia pastoris GS115; phylogenetic tree, expression in Pichia pastoris GS115, molecular mechanisms underlying the elevated expression of fatty acid desaturases induced by a decrease in the environmental temperature
expressed in Pichia pastoris strain GS115
Q3LU33;
expressed in Saccharomyces cerevisiae
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expressed in Saccharomyces cerevisiae strain BY4741, two different mRNA variants
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expressed in Saccharomyces cerevisiae strain InvSc1
expressed in Saccharomyces cerevisiae strain InvSc1; expression in Saccharomyces cerevisiae
expressed in Saccharomyces cerevisiae strain INVScl
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expressed in Saccharomyces cerevisiae, strain DBY746 with and without supplementation with linoleic acid
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expression in MCF7 cells
expression in Saccharomyces cerevisaiae
expression in Saccharomyces cerevisiae
expression of N-terminal truncated enzyme in Escherichia coli
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expression of wild-type, A181T/A188G/Y189F/S205N/L206T/G207A, A188G/Y189F, A181T/A200F and A181T/A200F/S205N/L206T/G207A mutant enzyme in Escherichia coli
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gene D6, recombinant expression in Saccharomyces
gene d6-des, DNA and amino acid sequence determination and analysis, sequence comparisons
gene D6DES, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, functional expression in Saccharomyces cerevisiae strain INVSc1 producing gamma-linolenic acid and stearidonic acid at conversion rates of 26.3-35.6% from exogenous linoleic acid and alpha-linolenic acid substrates, respectively. Fatty acid profiles of GC analysis from transgenic Saccharomyces cerevisiae strain INVSc1, overview
A0A1S5R926;
gene DELTA6fad_a, several variants, genetic structure, DNA and amino acid sequence determination and analysis, phylogenetic analysis, expression in Saccharomyces cerevisiae; gene DELTA6fad_b, several variants, genetic structure, DNA and amino acid sequence determination and analysis, phylogenetic analysis, expression in Saccharomyces cerevisiae; gene DELTA6fad_c, several variants, genetic structure, DNA and amino acid sequence determination and analysis, phylogenetic analysis, expression in Saccharomyces cerevisiae
D2KE02;, D2KE03;, Q6SES0;
gene desD, functional analysis of the Spirulina promoter in Escherichia coli, the -10 sequence, TATAAT, located at -33 bp relative to the translation start site, is essential for D6D promoter function, an ‘AT-rich inverted repeat’ -192 to -164 serves as a target-binding site for a transcriptional regulator
Q54795;
gene desI, recombinant expression in Saccharomyces
gene fads2, DNA and amino acid sequence determination and analysis, cloning of two alternative splicing transcripts named fads2-AS1 and fads2-AS2, quantitative real-time PCR expression analysis, recombinant expression in yeast, which shows fully functional DELTA6 desaturation activity toward C18 polyunsaturated fatty acid substrates, without residual DELTA5 and DELTA8 desaturase activities
gene FADS2, rs174616 genotype, genotyping
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gene FADS6, sequence comparisons, recombinant expression of wild-type and mutant enzymes in Saccharomyces cerevisiae strain INVSc1, subcloning in Escherichia coli Top 10 cells
gene fadsd6, real-time PCR enzyme expression and copy number analysis, recombinant expression in Danio rerio. The eicosapentaenoic acid (EPA) content is 1.9fold higher in F2 transgenic delta-6 desaturase transgenic zebrafish than in wild-type fish, the fish exhibiting FADS6 enzyme expression are bigger than wild-type fish. henotype, overview. By 48 h post-infection with Vibrio alginolyticus, expression of IL-10 gene is 3.3fold higher in delta-6 desaturase transgenic fish than in wild-type fish. Expression of TLR1, TLR3, TLR4, TRAM, and NF-kappaB is also significantly different between the transgenic and wild-type fish
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gene fat-3, quantitative real-time PCR expression analysis, overview
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gene Md6, DNA and amino acid sequence determination and analysis, Md6 promoter analysis in the 5'-upstream sequence, gene Md6 contains several eukaryotic fundamental transcription regulatory elements, sequence comparisons, functional recombinant expression in Saccharomyces cerevisiae strain INVSc1, the enzyme expression renders the yeast cells capable of converting linolenic acid to gamma-linolenic acid. The activity of DELTA6-desaturase increases by 2.8fold and 2.5fold when the mutant eMd6 sequence is placed upstream of -434 with forward or reverse orientations, respectively. The wild-type promoter of Md6 from Mucor sp. is a very strong promoter for DELTA6-desaturase and the sequence between -919 to -784 bp is an enhancer for DELTA6-desaturase activity
gene ObD6Des, DNA and amino acid sequence determination and analysis, sequence comparisons, functional expression in Saccharomyces cerevisiae strain W303-a
gene PiDesD6, DNA and amino acid sequence determination and analysis, phylogenetic analysis, functional expression in Saccharomyces cerevisiae strain W303, real-time quantitative PCR expression analysis
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human sequence determined
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plasmid coding for rat delta6-desaturase constructed using pCMV for expression in mammalian cells, rat delta6-desaturase sequence, GenBank accession number AB02 1980 PCR amplified, expressed by transiently transforming COS-7 cells
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recombinant overexpression of MpFADS6 in a uracil-auxotrophic Mortierella alpina strain to enhance eicosapentaenoic acid production in Mortierella alpina by favoring the omega3 pathway, using the Agrobacterium tumefaciens-mediated transformation method. The expression of MpFADS6 results in a 26.2fold increase in EPA production compared to wild-type Mortierella alpina
RT-PCR analysis of INS-1 beta-cell content of mRNA, primer pairs basedon known rat sequence
-
Saccharomyces cerevisiae transformed with fungal DELTA6-desaturase gene
-
transformed into Agrobacterium tumefaciens and expressed in Glycine max
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H129G
-
expressed in Saccharomyces cerevisiae, grown in SD medium in the presence of 50 microM of linoleic acid substrate, no enzyme activity, can be rescued by 150 mM exogenous imidazole
H129R
-
expressed in Saccharomyces cerevisiae, grown in SD medium in the presence of 50 microM of linoleic acid substrate, no enzyme activity using linoleic acid as substrate
H305G
-
expressed in Saccharomyces cerevisiae, grown in SD medium in the presence of 50 microM of linoleic acid substrate, no enzyme activity, can be rescued by 150 mM exogenous imidazole
H305R
-
expressed in Saccharomyces cerevisiae, grown in SD medium in the presence of 50 microM of linoleic acid substrate, no enzyme activity using linoleic acid as substrate
H89G
-
expressed in Saccharomyces cerevisiae, grown in SD medium in the presence of 50 microM of linoleic acid substrate, very low enzyme activity, can be rescued by 150 mM exogenous imidazole
H89R
-
expressed in Saccharomyces cerevisiae, grown in SD medium in the presence of 50 microM of linoleic acid substrate, very low enzyme activity using linoleic acid as substrate
H129G
-
expressed in Saccharomyces cerevisiae, grown in SD medium in the presence of 50 microM of linoleic acid substrate, no enzyme activity, can be rescued by 150 mM exogenous imidazole
-
H129R
-
expressed in Saccharomyces cerevisiae, grown in SD medium in the presence of 50 microM of linoleic acid substrate, no enzyme activity using linoleic acid as substrate
-
H305G
-
expressed in Saccharomyces cerevisiae, grown in SD medium in the presence of 50 microM of linoleic acid substrate, no enzyme activity, can be rescued by 150 mM exogenous imidazole
-
H89G
-
expressed in Saccharomyces cerevisiae, grown in SD medium in the presence of 50 microM of linoleic acid substrate, very low enzyme activity, can be rescued by 150 mM exogenous imidazole
-
H89R
-
expressed in Saccharomyces cerevisiae, grown in SD medium in the presence of 50 microM of linoleic acid substrate, very low enzyme activity using linoleic acid as substrate
-
D313I
site-directed mutagenesis, mutant shows slightly reduced activity compared to the wild-type enzyme
D367H
site-directed mutagenesis, mutant shows similar activity compared to the wild-type enzyme
F310L
site-directed mutagenesis, mutant shows similar activity compared to the wild-type enzyme
I390L
site-directed mutagenesis, mutant shows similar activity with linoleoyl-CoA and reduced activity with alpha-linolenoyl-CoA compared to the wild-type enzyme
M384S/M385L
site-directed mutagenesis, mutant shows significantly increased activity compared to the wild-type enzyme
N388H
site-directed mutagenesis, mutant shows similar activity compared to the wild-type enzyme
S306T
site-directed mutagenesis, mutant shows similar activity compared to the wild-type enzyme
S322A
site-directed mutagenesis, mutant shows highly increased activity compared to the wild-type enzyme
T302V
site-directed mutagenesis, mutant shows highly increased activity compared to the wild-type enzyme; site-directed mutagenesis, mutant shows potently increased activity compared to the wild-type enzyme
Y375F
site-directed mutagenesis, mutant shows significantly increased activity compared to the wild-type enzyme
E222S
site-directed mutagenesis, the mutant's relative conversion rate of alpha-linolenoyl-CoA is reduced by almost 50% compared to the wild-type enzyme
G194L
site-directed mutagenesis, the mutant's relative conversion rate of alpha-linolenoyl-CoA is significantly reduced to 6.50% compared to the wild-type enzyme
M227K
site-directed mutagenesis, the mutant's relative conversion rate of alpha-linolenoyl-CoA is reduced by almost 50% compared to the wild-type enzyme
Q209G
site-directed mutagenesis, the mutation does not lead to major changes in substrate preference
S197Q
site-directed mutagenesis, the mutation does not lead to major changes in substrate preference
V189L/Q190A
site-directed mutagenesis, the mutation does not lead to major changes in substrate preference
V399I/I400E
site-directed mutagenesis, the mutant's relative conversion rate of alpha-linolenoyl-CoA is reduced by almost 50% compared to the wild-type enzyme
G194L
-
site-directed mutagenesis, the mutant's relative conversion rate of alpha-linolenoyl-CoA is significantly reduced to 6.50% compared to the wild-type enzyme
-
M227K
-
site-directed mutagenesis, the mutant's relative conversion rate of alpha-linolenoyl-CoA is reduced by almost 50% compared to the wild-type enzyme
-
S197Q
-
site-directed mutagenesis, the mutation does not lead to major changes in substrate preference
-
V189L/Q190A
-
site-directed mutagenesis, the mutation does not lead to major changes in substrate preference
-
G390D
-
amino acid replacement in isoenzyme DELTA6I of DELTA6 desaturase-defective mutant strain YB214
T375K
-
amino acid replacement in isoenzyme DELTA6I of DELTA6 desaturase-defective mutant strain HR95
W314Stop
-
amino acid replacement in isoenzyme DELTA6I of DELTA6 desaturase-defective mutant strain ST66
A361Q
activity is significantly lower than that of wild-type enzyme
DELTA238P/DELTA239L
activity is significantly lower than that of wild-type enzyme; decreased or null DELTA6 desaturase activity
F166V/V167L
activity is significantly lower than that of wild-type enzyme
F356V/S358T
activity is significantly lower than that of wild-type enzyme
H410Y/E413K
activity is significantly lower than that of wild-type enzyme
I192T
activity is significantly lower than that of wild-type enzyme
K234N/S235M/L236delta
decreased or null DELTA6 desaturase activity
K234N/S235M/L236DELTA/K444Q
activity is significantly lower than that of wild-type enzyme
K444Q
decreased or null DELTA6 desaturase activity
N156T/A305V/Y182F/K234N/S235M/E365K/F166V/L423F/L424A/I195L/W245V
acquisition of DELTA5 desaturase activity without losing DELTA6 desaturase activity
N156T/A305V/Y182F/K234N/S235M/E365K/F166V/L423F/L424A/L248V/F322L/L323F/I195L/W245V
acquisition of DELTA5 desaturase activity without losing DELTA6 desaturase activity
N156T/A305V/Y182F/K234N/S235M/E365K/F166V/L423F/L424A/L248V/F322L/L323F/I195L/W245V/L396Y/V344P
acquisition of DELTA5 desaturase activity without losing DELTA6 desaturase activity
N156T/A305V/Y182F/K234N/S235M/E365K/F166V/L423F/L424A/L248V/F322L/L323F/I195L/W245V/L396Y/Y257H
acquisition of DELTA5 desaturase activity without losing DELTA6 desaturase activity
N156T/A305V/Y182F/K234N/S235M/E365K/F166V/L423F/L424A/L248V/F322L/L323F/I195L/W245V/L396Y/Y257H/V344P/I284F
acquisition of DELTA5 desaturase activity without losing DELTA6 desaturase activity
N156T/A305V/Y182F/K234N/S235M/E365K/F166V/L423F/L424A/L248V/F322L/L323F/I195L/W245V/L396Y/Y257H/V344P/I284F/F370A/I326V
acquisition of DELTA5 desaturase activity without losing DELTA6 desaturase activity
N156T/A305V/Y182F/K234N/S235M/E365K/F166V/L423F/L424A/L248V/F322L/L323F/I195L/W245V/L396Y/Y257H/V344P/I284F/F370A/Y352N
acquisition of DELTA5 desaturase activity without losing DELTA6 desaturase activity
N156T/A305V/Y182F/K234N/S235M/E365K/F166V/L423F/L424A/L248V/F322L/L323F/I195L/W245V/L396Y/Y257H/V344P/I284F/F370A/Y352N/I326V/Y188F/K190T
acquisition of DELTA5 desaturase activity without losing DELTA6 desaturase activity
N156T/A305V/Y182F/K234N/S235M/E365K/F166V/L423F/L424A/L248V/F322L/L323F/I195L/W245V/L396Y/Y257H/V344P/I284F/F370A/Y352N/I326V/Y188F/K190T/H410Y
acquisition of DELTA5 desaturase activity without losing DELTA6 desaturase activity
N156T/A305V/Y182F/K234N/S235M/E365K/F166V/L423F/L424A/L248V/F322L/L323F/I195L/W245V/L396Y/Y257H/V344P/I284F/F370A/Y352N/I326V/Y188F/K190T/H410Y/E413K
acquisition of DELTA5 desaturase activity without losing DELTA6 desaturase activity
N156T/A305V/Y182F/K234N/S235M/E365K/F166V/L423F/L424A/L248V/F322L/L323F/I195L/W245V/L396Y/Y257H/V344P/I284F/Y352N/I326V/H410Y
acquisition of DELTA5 desaturase activity without losing DELTA6 desaturase activity
N156T/A305V/Y182F/K234N/S235M/E365K/F166V/L423F/L424A/L248V/F322L/L323F/W245V
acquisition of DELTA5 desaturase activity without losing DELTA6 desaturase activity
P246S/L247V/Y249L
activity is significantly lower than that of wild-type enzyme
Q415E/E416S
activity is significantly lower than that of wild-type enzyme; decreased or null DELTA6 desaturase activity
R216M
activity is significantly lower than that of wild-type enzyme; decreased or null DELTA6 desaturase activity
S209P/N211S
activity is significantly lower than that of wild-type enzyme; decreased or null DELTA6 desaturase activity
Y352N/R353V
activity is significantly lower than that of wild-type enzyme
H360D
site-directed mutagenesis, mutant shows slightly reduced activity compared to the wild-type enzyme
H381N
site-directed mutagenesis, mutant shows slightly reduced activity compared to the wild-type enzyme
I306L
site-directed mutagenesis, mutant shows slightly reduced activity compared to the wild-type enzyme
L303F
site-directed mutagenesis, mutant shows slightly reduced activity compared to the wild-type enzyme
L383I
site-directed mutagenesis, mutant shows slightly reduced activity compared to the wild-type enzyme
M384S/M385
site-directed mutagenesis, mutant shows reduced activity compared to the wild-type enzyme
S322A
site-directed mutagenesis, mutant shows reduced activity compared to the wild-type enzyme
T299S
site-directed mutagenesis, mutant shows slightly reduced activity compared to the wild-type enzyme
T302V
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Y375F
site-directed mutagenesis, mutant shows reduced activity compared to the wild-type enzyme
A181T/A188G/Y189F/S205N/L206T/G207A
-
compared to wild-type: reduced DELTA6 desaturase activity with palmitoyl-[acyl-carrier protein] as substrate, strong DELTA9 desaturase activity with stearoyl-[acyl-carrier protein] as substrate, exhibits DELTA9 desaturase activity with palmitoyl-[acyl-carrier protein] as substrate
A181T/A200F
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increase in DELTA6 desaturase activity with palmitoyl-[acyl-carrier protein] as substrate, strong DELTA9 desaturase activity with stearoyl-[acyl-carrier protein] as substrate
A181T/A200F/S205N/L206T/G207A
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reduced DELTA6 desaturase activity with palmitoyl-[acyl-carrier protein] as substrate, very low DELTA9 desaturase activity, no DELTA6 desaturase activity with stearoyl-[acyl-carrier protein] as substrate
A188G/Y189F
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reduced DELTA6 desaturase activity with palmitoyl-[acyl-carrier protein] as substrate
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
diagnostics
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higher delta-6-desaturase activity is associated with a higher risk of developing metabolic syndrome
drug development
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the enzyme is a biological target for the discovery and development of pharmaceuticals to treat atherosclerosis
nutrition
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evaluating D6D activity in preterm infants is important for better nutritional management
synthesis
Show AA Sequence (240 entries)
Please use the Sequence Search for a specific query.